BIOE Exam 1 Study Guide
BIOE Exam 1 Study Guide BIOE 1010
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This 9 page Study Guide was uploaded by Sara Littlejohn on Sunday January 31, 2016. The Study Guide belongs to BIOE 1010 at Clemson University taught by Dr. Vladimir Reukov in Spring 2016. Since its upload, it has received 166 views. For similar materials see Biology for BioEngineers in Bioengineering at Clemson University.
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Date Created: 01/31/16
BIOE 1010 Exam 1 Study Guide Introduction : Cells-the fundamental units of life: *Water makes all of the complex Types of Cells: chemical reactions of life possible. o Eukaryotic Cells: Have a distinct nucleus Animal cells and plant cells o Prokaryotic Cells: No nucleus Bacteria More than 2000 chemical reactions take place in a cell every second; many of them are mutually incompatible. Cells developed strategies to keep reactions isolated and organized in separate compartments. In the cell there are membrane-enclosed compartments with specific functions. Examples of cell types: o Cardiac muscle cells (cardio myocytes): responsible for heartbeat o Endothelial cells: line and protect the lumen of blood vessels o Fibroblasts: synthesize proteins and are responsible for scar tissue o Red blood cells: transport and deliver oxygen to the tissues. Their shape provides a larger surface area so they can carry more oxygen. o White blood cells: protect the body against infections o Neurons: the core components of the nervous systems o Chondrocytes: cells in cartilage Looking at living cells: o Light Microscopy: magnifies cells up to 1000x and resolves details as small as 0.2 um. Can see no internal details o Florescence Microscopy: cells are treated with fluorescent dyes, which absorb light at one wavelength and emit it at another, longer wavelength. Contains two filters o ConfocalMicroscopy: builds an image by scanning the specimen with a laser beam Generates a sharp 3D image Florescent with specific details o Transmission ElectronMicroscopy: uses a beam of electrons instead of a beam of light and magnetic coils. The specimen in stained with electron dense heavy metals that absorb electrons. Can resolve details as small as 2 nm Can even see a portion of a long DNA molecule Sample has to be at a very low temp Has to be used in an vacuum o Scanning ElectronMicroscopy (SEM): the specimen is covered with a film of heavy metal and is scanned by a beam of electrons. Creates a 3D image Can resolve details between 3-20 nm How big is a cell? 5-20 um Proteins: structure and functions Chemistry Overview: Matter is made of combinations of elements Elements are substances that cannot be converted into other substances An atom is the smallest particle of an element that still remains its distinctive chemical properties. A molecule is a particle formed by the chemical union of two or more atoms. To achieve a complete outermost shell (the electron configuration of noble gases), unstable atoms tend to gain, lose, or share valence electrons with other atoms participate in chemical reactions and form molecules. The outermost electrons determine how atoms interact Sharing of electrons: covalent bonds Transfer of electrons: ionic bonds Common biological functional groups: Proteins: Proteins are long chains of amino acids and account for 20% of our bodies. Amino acids are grouped according to whether R is polar (hydrophilic) or non- polar (hydrophobic). Amino acid molecules react and form peptide bonds. Three amino acids joined by peptide bonds and form a tripeptide. Polypeptides = Proteins The 4 levels of organization: o Primary Structure: the sequence of amino acids that make up the polypeptide chain o Secondary Structure: can take the form of an alpha-helix or a beta-sheet which are maintained by hydrogen bonds between amino acids. o Tertiary Structure: the folding and bonding of the secondary structure. o Quaternary Structure: occurs as a result of interactions between twoor more tertiary subunits. An oligomeric protein is a complex of more than 1 chain that interact with each other. When the protein folds into its specific 3Dconformation amino acids which belong to different regions of the polypeptide chain are brought together to form a cavity with a unique geometry (bondingsite). Binding sites allow a protein to interact with its specific ligand. ProteinClassification (by function): o Structural: collagen, elastin o Chemical Messengers: hormones, growth factors o Transport: hemoglobin, myoglobin, lipoproteins o Contractile: actin, myosin o Protection: thrombin. Fibrinogen, antibodies o Signaling: receptors o Cell Adhesion: integrins o Catalytic: enzymes Enzymes are themost highly specialized proteins o They catalyze the conversion of substrate molecules into products o Are not consumed by the reactions they catalyze Active Catalytic Sites: pockets lined with amino acids that binds the substrate with great specificity and catalyze their chemical transformation. Induced-fit Model: both enzyme and substrate undergo dynamic conformational changes upon binding. Carbohydrates and Cell Metabolism: Carbohydrates: Carbs contain carbon, hydrogen, and oxygen They are the most abundant biomolecules on earth Roles: The main energy source for the human body Protect the cell form mechanical and chemical damage Absorb water-lubricate skeletal joints Participate in cell-cell recognition and adhesion processes Monosaccharides: the simplest type of sugars Pentoses- contain 5 carbons Hexoses- contain 6 carbons Open-chain structures: contain many hydroxyl groups and a carbonyl group (aldehyde or ketone) Ring/Cyclic structures formin water. Disaccharides: two monosaccharides covalently linked ( glycosidic bond) Examples: Sucrose (table sugar) and Lactose (milk sugar) THIS DIAGRAM WILL BE ON EXAM! KNOW WHAT THE GLYCOSIDIC BOND IS. Polysaccharides: polymers consisting of chains of monosaccharide units Glycogen (Poly glucose): the main storage polysaccharide of animal cells, especially abundant in the liver and skeletal muscle. Energy and Cell Metabolism: To go from the building blocks to larger units, cells need energy. Anabolism: biosynthesis of cellspecific molecules using the ANABOLISM AND energy harnessed formcatabolism CATABOLISM WILL BE ON Catabolism: breakdown of food molecules generating energy THE EXAM! and small molecules (building blocks) Energy is released by gradual oxidation of sugars and fats. Energy is transferred to carrier molecules (ATP and NADH) which store it temporarily in energy-rich bonds. ATP contains two high energy bonds. ATP provides the energy for synthesis of proteins, nucleic acids, fats, etc. The 2 types of reactions (releasing and requiring energy) are coupled by enzymes in many steps. In the cell, groups of enzymes work together: the product of METABOLIC one enzymatic reaction becomes substrate for the next one. PATHWAY IS This is called a metabolic pathway. ON EXAM! Glycolysis occursin the cytosol (cytoplasm). The first halfof glycolysis uses 2 ATP but it gains 2 NADH molecules and 4ATP in theend. Thedifference between NAD+ and NADH is NADH has an extra hydrogen bond and two more electrons than NAD+. ATP synthesis takes place in the mitochondria. Cells form ATP by complete oxidation of nutrient molecules in many small steps so that most of the energy released can be stored.
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